ID RAD52_MOUSE Reviewed; 420 AA. AC P43352; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 165. DE RecName: Full=DNA repair protein RAD52 homolog; GN Name=Rad52; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=7829098; DOI=10.1006/geno.1994.1503; RA Bendixen C., Sunjevaric I., Bauchwitz R., Rothstein R.; RT "Identification of a mouse homologue of the Saccharomyces cerevisiae RT recombination and repair gene, RAD52."; RL Genomics 23:300-303(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/HeJ; RX PubMed=7774919; DOI=10.1016/0888-7543(95)80126-7; RA Shen Z., Denison K., Lobb R., Gatewood J.M., Chen D.J.; RT "The human and mouse homologs of the yeast RAD52 gene: cDNA cloning, RT sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA RT expression in mouse tissues."; RL Genomics 25:199-206(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus; RX PubMed=7526206; DOI=10.1016/0921-8777(94)90040-x; RA Muris D.F., Bezzubova O., Buerstedde J.-M., Vreeken K., Balajee A.S., RA Osgood C.J., Troelstra C., Hoeijmakers J.H., Ostermann K., Schmidt H., RA Natarajan A.T., Eeken J.C.J., Lohman P.H.M., Pastink A.; RT "Cloning of human and mouse genes homologous to RAD52, a yeast gene RT involved in DNA repair and recombination."; RL Mutat. Res. 315:295-305(1994). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RA Sunjevaric I., Bendixen C., Mortensen U.H., Miljkovic V., Rothstein R.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in double-stranded break repair. Plays a central CC role in genetic recombination and DNA repair by promoting the annealing CC of complementary single-stranded DNA and by stimulation of the RAD51 CC recombinase. {ECO:0000250|UniProtKB:P43351}. CC -!- SUBUNIT: The full-length protein forms heptameric rings. Interacts with CC ABL1. Interacts with RPA2; the interaction is direct and associates CC RAD52 with the RPA complex. Interacts with RAD51AP1. CC {ECO:0000250|UniProtKB:P43351}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- PTM: Phosphorylated upon DNA damage by ABL1, and probably by ATM or CC ATR. {ECO:0000250|UniProtKB:P43351}. CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U06837; AAA75441.1; -; mRNA. DR EMBL; U12135; AAA85794.1; -; mRNA. DR EMBL; Z32767; CAA83659.1; -; mRNA. DR EMBL; AF004854; AAB69174.1; -; Genomic_DNA. DR CCDS; CCDS51887.1; -. DR PIR; A55727; A55727. DR PIR; A56529; A56529. DR RefSeq; NP_001159853.1; NM_001166381.2. DR AlphaFoldDB; P43352; -. DR SMR; P43352; -. DR FunCoup; P43352; 1547. DR STRING; 10090.ENSMUSP00000125502; -. DR GlyGen; P43352; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P43352; -. DR PhosphoSitePlus; P43352; -. DR PaxDb; 10090-ENSMUSP00000125502; -. DR ProteomicsDB; 255072; -. DR Antibodypedia; 10276; 432 antibodies from 38 providers. DR DNASU; 19365; -. DR Ensembl; ENSMUST00000162461.7; ENSMUSP00000125502.2; ENSMUSG00000030166.15. DR GeneID; 19365; -. DR KEGG; mmu:19365; -. DR UCSC; uc009dmq.2; mouse. DR AGR; MGI:101949; -. DR CTD; 5893; -. DR MGI; MGI:101949; Rad52. DR VEuPathDB; HostDB:ENSMUSG00000030166; -. DR eggNOG; KOG4141; Eukaryota. DR GeneTree; ENSGT00390000008766; -. DR InParanoid; P43352; -. DR OrthoDB; 206565at2759; -. DR PhylomeDB; P43352; -. DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ). DR BioGRID-ORCS; 19365; 7 hits in 115 CRISPR screens. DR PRO; PR:P43352; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P43352; protein. DR Bgee; ENSMUSG00000030166; Expressed in ascending aorta and 235 other cell types or tissues. DR ExpressionAtlas; P43352; baseline and differential. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISO:GO_Central. DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; ISO:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:MGI. DR GO; GO:0006974; P:DNA damage response; ISO:MGI. DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:CACAO. DR GO; GO:0000730; P:DNA recombinase assembly; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI. DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; ISO:MGI. DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central. DR FunFam; 3.30.390.80:FF:000001; DNA repair protein RAD52 homolog; 1. DR Gene3D; 3.30.390.80; DNA repair protein Rad52/59/22; 1. DR InterPro; IPR004585; DNA_recomb/repair_Rad52. DR InterPro; IPR041247; Rad52_fam. DR InterPro; IPR007232; Rad52_Rad59_Rad22. DR InterPro; IPR042525; Rad52_Rad59_Rad22_sf. DR NCBIfam; TIGR00607; rad52; 1. DR PANTHER; PTHR12132; DNA REPAIR AND RECOMBINATION PROTEIN RAD52, RAD59; 1. DR PANTHER; PTHR12132:SF1; DNA REPAIR PROTEIN RAD52 HOMOLOG; 1. DR Pfam; PF04098; Rad52_Rad22; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. PE 2: Evidence at transcript level; KW DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..420 FT /note="DNA repair protein RAD52 homolog" FT /id="PRO_0000173882" FT DNA_BIND 153..157 FT /evidence="ECO:0000250" FT REGION 222..291 FT /note="Mediates interaction with RPA2" FT /evidence="ECO:0000250" FT REGION 357..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..368 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..420 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 105 FT /note="Phosphotyrosine; by ABL1" FT /evidence="ECO:0000250|UniProtKB:P43351" FT MOD_RES 200 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P43351" FT MOD_RES 339 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P43351" FT CONFLICT 195 FT /note="E -> K (in Ref. 2; AAA85794)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="Missing (in Ref. 2; AAA85794)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="A -> G (in Ref. 1 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="Missing (in Ref. 1 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="D -> N (in Ref. 3; CAA83659)" FT /evidence="ECO:0000305" SQ SEQUENCE 420 AA; 46910 MW; 84514C8579072F98 CRC64; MAGPEEAVHR GCDNHPPFVG GKSVLLFGQS QYTADEYQAI QKALRQRLGP EYISSRMAGG GQKVCYIEGH RVINLANEMF GYNGWAHSIT QQNVDFVDLN NGKFYVGVCA FVKVQLKDGS YHEDVGYGVS EGLRSKALSL EKARKEAVTD GLKRALRSFG NALGNCILDK DYLRSLNKLP RQLPLDVDLT KTKREDFEPS VEQARYNSCR QNEALGLPKP QEVTSPCRSS PPHDSNIKLQ GAKDISSSCS LAATLESDAT HQRKLRKLRQ KQLQQQFREQ METRRQSHAP AEEVAAKHAA VLPAPPKHST PVTAASELLQ EKVVFPDNLE ENLEMWDLTP DLEDIIKPLC RAEPAQTSAT RTFNNQDSVP HIHCHQKPQE KPGPGHLQTC NTNQHVLGSR EDSEPHRKSQ DLKKRKLDPS //